Carboxypeptidase M is an
enzyme that in humans is encoded by the CPMgene.[5][6]
Function
The protein encoded by this gene is a membrane-bound arginine/lysine
carboxypeptidase. Its
expression is associated with
monocyte to
macrophage differentiation. This encoded protein contains
hydrophobic regions at the amino and carboxy termini and has 6 potential
asparagine-linked
glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced
transcript variants encoding the same protein have been described for this gene.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Kas K, Schoenmakers EF, Van de Ven WJ (November 1995). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics. 30 (2): 403–5.
PMID8586455.
Rehli M, Krause SW, Andreesen R (2000). "The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo". Cellular Peptidases in Immune Functions and Diseases 2. Advances in Experimental Medicine and Biology. Vol. 477. pp. 205–16.
doi:
10.1007/0-306-46826-3_23.
ISBN0-306-46383-0.
PMID10849748.
Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain and peripheral nerves". Journal of Neurochemistry. 59 (6): 2201–12.
doi:
10.1111/j.1471-4159.1992.tb10112.x.
PMID1431901.
S2CID19152354.
Nagae A, Abe M, Becker RP, Deddish PA, Skidgel RA, Erdös EG (August 1993). "High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells". American Journal of Respiratory Cell and Molecular Biology. 9 (2): 221–9.
doi:
10.1165/ajrcmb/9.2.221.
PMID8338689.
Michel B, Igić R, Leray V, Deddish PA, Erdös EG (April 1996). "Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M". Circulation Research. 78 (4): 635–42.
doi:
10.1161/01.res.78.4.635.
PMID8635221.
Skidgel RA, McGwire GB, Li XY (May 1996). "Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones". Immunopharmacology. 32 (1–3): 48–52.
doi:
10.1016/0162-3109(96)00008-2.
PMID8796265.
Li XY, Skidgel RA (April 1999). "Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis". Biochemical and Biophysical Research Communications. 258 (1): 204–10.
doi:
10.1006/bbrc.1999.0619.
PMID10222261.
Lendeckel U, Arndt M, Wrenger S, Nepple K, Huth C, Ansorge S, Klein HU, Goette A (June 2001). "Expression and activity of ectopeptidases in fibrillating human atria". Journal of Molecular and Cellular Cardiology. 33 (6): 1273–81.
doi:
10.1006/jmcc.2001.1389.
PMID11444929.
Carboxypeptidase M is an
enzyme that in humans is encoded by the CPMgene.[5][6]
Function
The protein encoded by this gene is a membrane-bound arginine/lysine
carboxypeptidase. Its
expression is associated with
monocyte to
macrophage differentiation. This encoded protein contains
hydrophobic regions at the amino and carboxy termini and has 6 potential
asparagine-linked
glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced
transcript variants encoding the same protein have been described for this gene.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Kas K, Schoenmakers EF, Van de Ven WJ (November 1995). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics. 30 (2): 403–5.
PMID8586455.
Rehli M, Krause SW, Andreesen R (2000). "The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo". Cellular Peptidases in Immune Functions and Diseases 2. Advances in Experimental Medicine and Biology. Vol. 477. pp. 205–16.
doi:
10.1007/0-306-46826-3_23.
ISBN0-306-46383-0.
PMID10849748.
Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain and peripheral nerves". Journal of Neurochemistry. 59 (6): 2201–12.
doi:
10.1111/j.1471-4159.1992.tb10112.x.
PMID1431901.
S2CID19152354.
Nagae A, Abe M, Becker RP, Deddish PA, Skidgel RA, Erdös EG (August 1993). "High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells". American Journal of Respiratory Cell and Molecular Biology. 9 (2): 221–9.
doi:
10.1165/ajrcmb/9.2.221.
PMID8338689.
Michel B, Igić R, Leray V, Deddish PA, Erdös EG (April 1996). "Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M". Circulation Research. 78 (4): 635–42.
doi:
10.1161/01.res.78.4.635.
PMID8635221.
Skidgel RA, McGwire GB, Li XY (May 1996). "Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones". Immunopharmacology. 32 (1–3): 48–52.
doi:
10.1016/0162-3109(96)00008-2.
PMID8796265.
Li XY, Skidgel RA (April 1999). "Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis". Biochemical and Biophysical Research Communications. 258 (1): 204–10.
doi:
10.1006/bbrc.1999.0619.
PMID10222261.
Lendeckel U, Arndt M, Wrenger S, Nepple K, Huth C, Ansorge S, Klein HU, Goette A (June 2001). "Expression and activity of ectopeptidases in fibrillating human atria". Journal of Molecular and Cellular Cardiology. 33 (6): 1273–81.
doi:
10.1006/jmcc.2001.1389.
PMID11444929.